Electrical impedance monitoring of protein unfolding

Lima, Sandro V. de; Melo, Celso P. de

doi:10.1039/c6ra20901g

Cited by 6 publications

(3 citation statements)

References 41 publications

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“…Change in the absorption spectrum of BSA due to interaction with SDS (Figure a) and a double logarithm plot (Figure b) helped to obtain the various stages of binding of the surfactant molecules with BSA and the consequent structural change of the protein. The consecutive linear stages in Figure b can be identified as the regions of binding (specific, non-cooperative, and cooperative) . Shifts in the corresponding fluorescence emission maxima of the BSA sample due to interactions with SDS monomers/aggregates at different stages clearly indicate difference in structural forms of the protein (Figure ).…”

Section: Resultsmentioning

confidence: 98%

“…The consecutive linear stages in Figure 1b can be identified as the regions of binding (specific, non-cooperative, and cooperative). 22 Shifts in the corresponding fluorescence emission maxima of the BSA sample due to interactions with SDS monomers/aggregates at different stages clearly indicate difference in structural forms of the protein (Figure 2). 22 The interaction between C6 (1 μM) aggregates and BSA in aqueous medium provides interesting results.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…22 Shifts in the corresponding fluorescence emission maxima of the BSA sample due to interactions with SDS monomers/aggregates at different stages clearly indicate difference in structural forms of the protein (Figure 2). 22 The interaction between C6 (1 μM) aggregates and BSA in aqueous medium provides interesting results. In this experiment, the concentration of C6 was kept fixed and enough time was provided for C6 to form microaggregates.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Piecemeal Rekindling of Coumarin 6 Fluorescence on Stepwise Unfolding of Protein by Surfactant

Banerjee

Purkayastha

2017

J. Phys. Chem. B

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Coumarin 6 (C6) briskly aggregates in water, and as a result, rapidly loses fluorescence. However, vicinal hydrophobic cavity can induce disintegration of the aggregates, and thus reviving the fluorescence. It is shown that carrier protein, such as bovine serum albumin (BSA), can disintegrate the microcrystals of C6 to smaller fragments and trap them inside the hydrophobic domain of the folded protein. This results into a 12-fold enhancement in the fluorescence signal of C6. However, on unfolding BSA by micelles, the C6 microcrystals break into single molecules by getting trapped in the micelles, and hence emission enhances by more than 100-folds.

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Section: Resultsmentioning

confidence: 98%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

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Piecemeal Rekindling of Coumarin 6 Fluorescence on Stepwise Unfolding of Protein by Surfactant

Banerjee

Purkayastha

2017

J. Phys. Chem. B

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Carbamoylase-based impedimetric electronic tongue for rapid detection of paralytic shellfish toxins

Raposo,

Soreto,

Moreirinha

et al. 2024

Anal Bioanal Chem

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Phytotoxins produced by marine microalgae, such as paralytic shellfish toxins (PSTs), can accumulate in bivalve molluscs, representing a human health concern due to the life-threatening symptoms they cause. To avoid the commercialization of contaminated bivalves, monitoring programs were established in the EU. The purpose of this work is the implementation of a PST transforming enzyme—carbamoylase—in an impedimetric test for rapid simultaneous detection of several carbamate and N-sulfocarbamoyl PSTs. Carbamoylase hydrolyses carbamate and sulfocarbamoyl toxins, which may account for up to 90% of bivalve toxicity related to PSTs. Conformational changes of carbamoylase accompanying enzymatic reactions were probed by Fourier transform mid-infrared spectroscopy (FT-MIR) and electrochemical impedance spectroscopy (EIS). Furthermore, a combination of EIS with a metal electrode and a carbamoylase-based assay was employed to harness changes in the enzyme conformation and adsorption on the electrode surface during the enzymatic reaction as an analytical signal. After optimization of the working conditions, the developed impedimetric e-tongue could quantify N-sulfocarbamoyl toxins with a detection limit of 0.1 µM. The developed e-tongue allows the detection of these toxins at concentration levels observed in bivalves with PST toxicity close to the regulatory limit. The quantification of a sum of N-sulfocarbamoyl PSTs in naturally contaminated mussel extracts using the developed impedimetric e-tongue has been demonstrated.

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Real-time monitoring of amyloid fibrillation by electrical impedance spectroscopy

Silva

Lima

Melo

et al. 2017

Colloids and Surfaces B: Biointerfaces

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Electrical impedance monitoring of protein unfolding

Abstract: We have applied electrical impedance spectroscopy (EIS) to investigate how the dielectric characteristics of protein aqueous solutions respond to varying amounts of a co-dissolved surfactant.

Cited by 6 publications

References 41 publications

Piecemeal Rekindling of Coumarin 6 Fluorescence on Stepwise Unfolding of Protein by Surfactant

Piecemeal Rekindling of Coumarin 6 Fluorescence on Stepwise Unfolding of Protein by Surfactant

Carbamoylase-based impedimetric electronic tongue for rapid detection of paralytic shellfish toxins

Real-time monitoring of amyloid fibrillation by electrical impedance spectroscopy

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